P38207 (APN2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA-(apurinic or apyrimidinic site) lyase 2
EC=4.2.99.18

Alternative name(s):
AP endonuclease 2
Apurinic-apyrimidinic endonuclease 2

Gene names

Name:	APN2
Synonyms:	ETH1
Ordered Locus Names:	YBL019W
ORF Names:	YBL0443

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	520 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	DNA repair enzyme that cleaves apurinic/apyrimidinic (AP) sites and removes 3'-blocking groups present at single strand breaks of damaged DNA.
Catalytic activity	The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate.
Cofactor	Magnesium. Can also utilize manganese. Probably binds two magnesium or manganese ions per subunit By similarity.
Subcellular location	Nucleus.
Miscellaneous	Present with 414 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the DNA repair enzymes AP/ExoA family.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Cellular component	Nucleus
Ligand	Magnesium Metal-binding
Molecular function	Lyase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	base-excision repair Inferred from genetic interaction Ref.4. Source: SGD
Cellular_component	nucleus Inferred by curator Ref.5. Source: SGD
Molecular_function	DNA binding Inferred from electronic annotation. Source: InterPro DNA-(apurinic or apyrimidinic site) lyase activity Inferred from direct assay Ref.5. Source: SGD double-stranded DNA specific 3'-5' exodeoxyribonuclease activity Inferred from direct assay PubMed 11238902. Source: SGD endonuclease activity Inferred from electronic annotation. Source: InterPro phosphoric diester hydrolase activity Inferred from direct assay PubMed 11238902. Source: SGD zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 520	520	DNA-(apurinic or apyrimidinic site) lyase 2		PRO_0000200020
Sites
	Active site	181	1	By similarity
	Active site	222	1	Proton donor/acceptor By similarity
	Metal binding	59	1	Magnesium 1 By similarity
	Metal binding	222	1	Magnesium 2 By similarity
	Metal binding	224	1	Magnesium 2 By similarity
	Metal binding	353	1	Magnesium 1 By similarity
	Site	224	1	Transition state stabilizer By similarity
	Site	328	1	Important for catalytic activity By similarity
	Site	354	1	Interaction with DNA substrate By similarity
Experimental info
	Sequence conflict	15	1	N → D in AAT93202. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P38207 [UniParc]. Last modified October 1, 1994. Version 1. Checksum: E3947C4D904C53FB	FASTA	520	59,445
	10 20 30 40 50 60 MSSSENTLLD GKSENTIRFL TFNVNGIRTF FHYQPFSQMN QSLRSVFDFF RADIITFQEL 70 80 90 100 110 120 KTEKLSISKW GRVDGFYSFI SIPQTRKGYS GVGCWIRIPE KNHPLYHALQ VVKAEEGITG 130 140 150 160 170 180 YLTIKNGKHS AISYRNDVNQ GIGGYDSLDP DLDEKSALEL DSEGRCVMVE LACGIVIISV 190 200 210 220 230 240 YCPANSNSSE EGEMFRLRFL KVLLRRVRNL DKIGKKIVLM GDVNVCRDLI DSADTLEQFS 250 260 270 280 290 300 IPITDPMGGT KLEAQYRDKA IQFIINPDTP HRRIFNQILA DSLLPDASKR GILIDTTRLI 310 320 330 340 350 360 QTRNRLKMYT VWNMLKNLRP SNYGSRIDFI LVSLKLERCI KAADILPDIL GSDHCPVYSD 370 380 390 400 410 420 LDILDDRIEP GTTQVPIPKF EARYKYNLRN HNVLEMFAKK DTNKESNKQK YCVSKVMNTK 430 440 450 460 470 480 KNSNIKNKSL DSFFQKVNGE KDDRIKESSE IPQQAKKRIS TPKLNFKDVF GKPPLCRHGE 490 500 510 520 ESMLKTSKTS ANPGRKFWIC KRSRGDSNNT ESSCGFFQWV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete DNA sequence of yeast chromosome II." Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C. , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K. EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[3]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	"Identification of APN2, the Saccharomyces cerevisiae homolog of the major human AP endonuclease HAP1, and its role in the repair of abasic sites." Johnson R.E., Torres-Ramos C.A., Izumi T., Mitra S., Prakash S., Prakash L. Genes Dev. 12:3137-3143(1998) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[5]	"Apurinic endonuclease activity of yeast Apn2 protein." Unk I., Haracska L., Johnson R.E., Prakash S., Prakash L. J. Biol. Chem. 275:22427-22434(2000) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[6]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z35780 Genomic DNA. Translation: CAA84838.1. AY693183 Genomic DNA. Translation: AAT93202.1. BK006936 Genomic DNA. Translation: DAA07101.1.
PIR	S45753.
RefSeq	NP_009534.1. NM_001178259.1.
3D structure databases
ProteinModelPortal	P38207.
SMR	P38207. Positions 17-365.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-3930N.
IntAct	P38207. 2 interactions.
MINT	MINT-515848.
STRING	4932.YBL019W.
Proteomic databases
PaxDb	P38207.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YBL019W; YBL019W; YBL019W.
GeneID	852262.
KEGG	sce:YBL019W.
Organism-specific databases
CYGD	YBL019w.
SGD	S000000115. APN2.
Phylogenomic databases
eggNOG	COG0708.
GeneTree	ENSGT00530000063540.
HOGENOM	HOG000246560.
KO	K10772.
OMA	MYTVWNT.
OrthoDB	EOG4GQTDH.
Gene expression databases
Genevestigator	P38207.
GermOnline	YBL019W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR020848. AP_endonuclease_F1_CS. IPR005135. Endo/exonuclease/phosphatase. IPR004808. ExoDNase_III. IPR010666. Znf_GRF. [Graphical view]
PANTHER	PTHR22748. PTHR22748. 1 hit.
Pfam	PF03372. Exo_endo_phos. 1 hit. PF06839. zf-GRF. 1 hit. [Graphical view]
SUPFAM	SSF56219. Exo_endo_phos. 1 hit.
PROSITE	PS00726. AP_NUCLEASE_F1_1. False negative. PS00727. AP_NUCLEASE_F1_2. False negative. PS00728. AP_NUCLEASE_F1_3. 1 hit. PS51435. AP_NUCLEASE_F1_4. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	970856.

Entry information

Entry name

APN2_YEAST

Accession

Primary (citable) accession number: P38207
Secondary accession number(s): D6VPY1, E9P926

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	May 1, 2013
This is version 102 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program